Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P43026 (lipopolysaccharide)
 62,215 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This study was carried out to determine whether bone might be a source of hemopoietic growth factors. Both neonatal murine calvaria and primary cultures of cells isolated from calvaria released, upon stimulation with lipopolysaccharide, an activity that stimulated the growth of the interleukin (IL) 3-dependent cell lines, 32D cl, 123, and NSF 60. Upon gel filtration, this activity eluted with a molecular weight of 30,000 kDa. Further characterization, however, revealed that the major activity in conditioned medium was not IL 3. Activity was absorbed by DEAE-Sephacel at low salt concentration, whereas IL 3 does not adhere. Furthermore, an IL 3-specific antiserum did not neutralize the activity from cells and only partly neutralized the activity generated by whole calvaria. After gel filtration, the 30-kDa activity stimulated the growth of very large colonies in semisolid medium consisting mainly of granulocytes with the remainder being macrophages. No colony types belonging to other hemopoietic lineages were found, indicating, again, that the activity was not identical to IL 3. Subsequently, conditioned medium was fractionated by hydrophobic chromatography on Phenyl-Sepharose CL-4B, yielding two peaks of activity. Neutralization of activity with antisera to granulocyte-macrophage colony-stimulating factor (GM-CSF) and IL 3 and use of colony assays showed that medium conditioned by whole calvaria contained GM-CSF and granulocyte CSF (G-CSF) in similar amounts together with a little IL 3, and medium conditioned with calvaria cells contained GM-CSF and little G-CSF. We conclude that bone releases hemopoietic growth factors that could contribute both to hemopoiesis and to the recruitment of osteoclasts from progenitors resident in the adjacent marrow.
 ...
PMID:Production of hemopoietic growth factors by bone tissue and bone cells in culture. 326 92

Experiments were conducted to purify the differentiation-inducing factor (D-factor), which induces differentiation of mouse myeloid leukemic cell line, Ml, into macrophage-like cells, in a conditioned medium of guinea pig peritoneal macrophages stimulated with lipopolysaccharide. On gel filtration under high performance liquid column chromatography (HPLC), D-factor eluted at the position of 45-15 KD. By the subsequent separation on DEAE HPLC the D-factor activity disappeared. However, in the presence of recombinant human IL 1 alpha the D-factor activity appeared at a position where tumor necrosis factor (TNF) eluted. Even after fractionation on hydroxyapatite HPLC the IL 1-dependent D-factor was co-chromatographed with TNF. Recombinant human TNF as well as the partially purified guinea pig TNF induced differentiation of Ml cells in conjunction with either the partially purified guinea pig IL 1 or recombinant human IL 1 alpha, although these factors by themselves did not induce differentiation. These findings suggest that a part of D-factor activity in the conditioned medium resulted from the cooperative effects between TNF and IL 1.
 ...
PMID:Tumor necrosis factor as an interleukin 1-dependent differentiation inducing factor (D-factor) for mouse myeloid leukemic cells. 349 76

Tumor necrosis factor (TNF) was detected in the sera of normal mice, unprimed by reticuloendothelial system (RES) stimulators, when such mice were injected with lipopolysaccharide (LPS). Amounts of TNF were approximately 200-fold less than those found in Corynebacterium parvum-primed mice. No TNF activity was detected in the sera of mice not administered LPS. TNF induction in unprimed mice was refractory to repeated administration of endotoxin, thus exhibiting a tolerance phenomenon. TNF produced in unprimed mice eluted similarly to Mycobacterium bovis, strain BCG-primed TNF on Sephacryl S-200 and DEAE Sephacel columns and was neutralized by rabbit antisera raised to partially purified BCG-primed TNF. When BALB/c mice having 7-day old subcutaneous Meth A tumor implants were administered TNF antiserum, endotoxin-induced hemorrhagic necrosis was largely prevented. These findings strongly suggest that endotoxin-induced hemorrhagic necrosis of tumors is mediated through TNF production and action.
 ...
PMID:Production of tumor necrosis factor in unprimed mice: mechanism of endotoxin-mediated tumor necrosis. 352 51

The binding characteristics of partially purified glucocorticoid receptor complexes from hormone sensitive, non-differentiating BCL1 cells to sequentially deproteinized BCL1 chromatin-cellulose was investigated. [3H]Triamcinolone acetonide (TA)-receptor complexes were purified (approx. 30-fold) from DEAE-cellulose columns by salt elution which allowed receptor activation only in the absence of molybdate. Addition of 10 mM molybdate completely blocked salt activation. The binding pattern of the activated [3H]TA-receptor complexes to chromatin-cellulose extracted with 0-8 M guanidine hydrochloride revealed three regions of increased binding activity (acceptor sites), at 2, 5 and 7 M guanidine hydrochloride. Acceptor site binding was markedly reduced for chromatin extracted with 3, 6 and 8 M guanidine hydrochloride. Non-activated receptor complexes demonstrated very low binding to deproteinized chromatin. It was also shown that chromatin binding required glucocorticoid receptors and that free ligand or ligand bound to other proteins did not bind significantly to chromatin. In addition, binding of [3H]TA-receptor complexes to partially deproteinized chromatin was competable by unlabeled TA-receptor complexes. Scatchard analysis demonstrated that chromatin from non-differentiating BCL1 cells possesses multiple, high-affinity binding sites which differ in their affinity for the glucocorticoid receptor. Partially deproteinized chromatin from lipopolysaccharide-stimulated BCL1 cells demonstrated a different pattern of receptor binding, i.e., receptor binding was significantly greater to chromatin previously extracted with 6-8 M guanidine hydrochloride. These results suggest that differentiation alters the state of chromatin and the interaction of non-histone protein/DNA acceptor sites with glucocorticoid receptors. These alterations may play a role in the acquisition of hormone resistance.
 ...
PMID:Binding of [3H]triamcinolone acetonide-receptor complexes to chromatin from the B-cell leukemia line, BCL1. 387 35

A Klebsiella pneumoniae serotype 2 strain was examined for its ability to produce extracellular toxic material. The organism was grown to the stationary phase in a defined medium, and the toxic material was isolated by ultrafiltration-ion-exchange chromatography on DEAE-Sephacel and gel filtration chromatography on Sepharose 4B or 2B. It was found to be comprised of 63% capsular polysaccharide, 30% lipopolysaccharide, and 7% protein and possessed a 50% lethal dose (when injected intraperitoneally into mice) of 393 +/- 45 micrograms. The toxicity appeared to be associated with the endotoxin portion of the compound, because boiling for 15 min and exposure to proteolytic enzymes had no effect on the toxicity. However, saponification destroyed the toxicity of the compound. Studies employing radial immunodiffusion examining the sera of mice infected with this organism demonstrated in vivo production of the complex at levels sufficiently high to produce death. When sublethal amounts of this complex were placed in the lungs of specific-pathogen-free mice, the lung pathology observed after 24, 48, and 72 h was similar to the damage caused by an active K. pneumoniae lobar pneumonia. These data indicate that this extracellular toxic compound produced by K. pneumoniae may be responsible for the lethality and lung tissue destruction normally associated with an active lobar pneumonia caused by this organism.
 ...
PMID:Importance of a lipopolysaccharide-containing extracellular toxic complex in infections produced by Klebsiella pneumoniae. 390 14

Partially purified water extract was obtained from the initial water extract by ultracentrifugation. Nine protein fractions differing in molecular weight, homogeneity and the content of lipopolysaccharide (LPS) were obtained by stepwise precipitation with ammonium sulfate and subsequent fractionation in columns packed with Sephadex G-100 and DEAE cellulose. Two protein fractions with a molecular weight of 30000 and 40000 daltons were practically free of LPS. These fractions were homogeneous as shown by analytical centrifugation and formed a single precipitation line with P. aeruginosa antiserum; both fractions were found to be antigenically identical. In the enzyme immunoassay these two fractions proved to be least active in comparison with the other protein fractions, but when used for the immunization of rabbits, they induced the formation of specific protective (for mice) antibodies. Both antisera were equally active in the experiments of the passive protection of mice. The isolated LPS-free proteins are supposed to be the proteins of the outer membrane of P. aeruginosa cell wall and have the properties of protective antigens.
 ...
PMID:[Protective protein antigens of Pseudomonas aeruginosa]. 393 89

Two polyclonal B cell activators, lipopolysaccharide (LPS) and poly I:C, have been used to induce interferon (IFN) production by murine B cell populations. The results show that splenic B cell-enriched fractions, isolated by wheat germ agglutination followed by C-dependent anti-Thy 1.2 cytolysis, respond to treatment with poly I:C + DEAE-dextran by IFN production at levels comparable on a per cell basis to unfractionated spleen cells. By contrast, the LPS-stimulated IFN response of these same B cell fractions is either undetectable or substantially lower than that of spleen cells; although the B cell fractions appear fully capable of LPS-induced proliferation. Consistent with this pattern of splenic B cell IFN responses, two antibody-secreting hybridoma lines and two myeloma cell lines (including the parental myeloma of the hybrid) can be stimulated by poly I:C + DEAE-dextran to produce IFN; yet these same B cell lines do not synthesize IFN in response to LPS at doses from 1-100 micrograms/ml. The level of poly I:C-induced IFN secreted by the hybridomas are approximately 10-fold greater than that produced by the unfused parental myeloma cells. Not only do these results directly demonstrate that murine lymphocytes of the B cell lineage produce IFN in response to the B cell activator poly I:C, but these observations also strongly suggest that the IFN responses of the B cell tumor lines model the IFN producing capacity of splenic B cells. Moreover, since the hybridoma cell lines and one of the myeloma lines synthesize specific antibody molecules, these observations show that the progeny of a single B cell clone can synthesize and secrete both IFN and immunoglobulin.
 ...
PMID:Differences in the B cell interferon responses to lipopolysaccharide and poly I:C. 618 67

A suppressive B-cell factor (SBF)-producing hybridoma termed TS-4.44 was established by fusion of B cells which possessed receptors for the Fc portion of IgG (FcR gamma + B cells) and thymidine kinase defective fibroblasts, 3T3-4E cells. The biological properties of hybridoma-produced SBF (Hyb-SBF) are almost the same as those of conventionally prepared SBF (Conv-SBF). Hyb-SBF suppresses (i) plaque-forming cell (PFC) responses in an antigen non-specific manner, (ii) DNA synthesis of lipopolysaccharide (LPS)-activated B cells, but neither concanavalin A (Con A) nor phytohaemagglutinin (PHA)-induced activation of T cells, and (iii) the proliferation of B, but not non-B tumour cells. Once absorbed with L-1210 cells, Hyb-SBF failed to inhibit both PFC and LPS responses. It is important is that Hyb-SBF suppresses the proliferation of L-1210 cells not only in vitro, but also in vivo. The physicochemical properties of Hyb-SBF such as sensitivity to trypsin, pronase and neuraminidase and its molecular weight (43,000), as judged by gel filtration and sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) are in accord with those of Conv-SBF. Moreover, it is eluted from a DEAE cellulose column with 0.1-0.3 M phosphate buffer. Thus, monoclonal SBF is thought to be identical with Conv-SBF and could provide us with sufficient material for the analysis of FcR-dependent immunoregulation including surveillance mechanisms controlling the proliferation of B tumour cells.
 ...
PMID:Monoclonal SBF produced by a hybridoma: in-vitro and in-vivo suppression of B tumour-cell proliferation. 636 Aug 50

Guinea pig monokines produced by lipopolysaccharide-stimulated peritoneal macrophages were found in high (50,000-80,000) and low (10,000-30,000) molecular weight (m.w.) fractions by gel filtration. Both showed enhancing activity on the proliferative response of guinea pig and mouse thymocytes to PHA, but the high m.w. (65K) monokine was much more efficient than the low m.w. (15K) monokine in enhancing the response of lymph node T cells to PHA, suggesting its importance in the activation of peripheral T cells. The 65K monokine was coeluted with BSA present in the culture medium by DEAE-cellulose chromatography, but was clearly separated from it by hydroxylapatite chromatography. The immunoadsorption experiment with anti-BSA-coupled gel also indicated that 65K monokine is not a complex of low m.w. monokine with BSA. Our series of studies showed that most monokine activities were always found in the 65K fraction in guinea pigs. Thus, in guinea pigs, the 65K component appears to constitute a major class of T cell-activating monokines.
 ...
PMID:T cell-activating monokines in guinea pigs: comparison of high and low molecular weight factors. 637 91

The lamB protein, the receptor for phage lambda, was purified from the outer membrane of Escherichia coli K-12 by extraction with Triton X-100 and EDTA, chromatography on DEAE-Sephacel in Triton X-100, exchange of Triton for cholate by gel filtration, and chromatography on Sephacryl S-200 in cholate, NaCl, and EDTA. The purified protein appeared to exist as several oligomeric species. In an equilibrium retention assay with reconstituted vesicles containing phospholipids and lipopolysaccharide, the lamB protein conferred permeability for disaccharides. In a liposome swelling assay designed to measure rates of diffusion, the lamB protein conferred permeability to phospholipid liposomes for a variety of substrates. The rates obtained indicate the permeation facilitated by the lamB protein is specific, discriminating among substrates by both size and configuration. For example, maltose diffused into liposomes 40 times faster than sucrose, about 8 times faster than cellobiose, and about 12 times faster than maltoheptaose. The results suggest that the lamB protein forms a transmembrane channel containing a site (or sites) that loosely interacts with the solutes.
 ...
PMID:Specificity of diffusion channels produced by lambda phage receptor protein of Escherichia coli. 644 20


<< Previous 1 2 3 4 5 6 7 Next >>